Simulations of a specific inhibitor of the dishevelled PDZ domain.
The dishevelled (Dvl) PDZ domain is believed to play an essential role in the canonical and noncanonical Wnt signaling pathways, which are involved in embryo development as well as in tumorigenesis. Also, it binds directly to frizzled (Fz) receptors. An organic molecule (NSC668036) from the National Cancer Institute small-molecule library has been identified to be able to bind to the Dvl PDZ domain. Molecular dynamics simulation was used to provide detailed analyses of the binding between them.
Chen
Xin
X
Department of Physics, Stony Brook University, Stony Brook, NY 11794, USA.
Deng
Yuefan
Y
D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D047630:Depsipeptides / Q000737:chemistry*; D000072261:Dishevelled Proteins; D047108:Embryonic Development / Q000502:physiology; D006571:Heterocyclic Compounds / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D054731:PDZ Domains; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D015398:Signal Transduction / Q000502:physiology; D051153:Wnt Proteins / Q000737:chemistry / Q000378:metabolism
D048868:Adaptor Proteins, Signal Transducing; D047630:Depsipeptides; D000072261:Dishevelled Proteins; D006571:Heterocyclic Compounds; C534585:NSC 668036; D010750:Phosphoproteins; D051153:Wnt Proteins